Selection of m. tuberculosis clinically isolated sensitive & resistant to fluoroquinolones


  • Sudhakar Kancharla Director Clinical Laboratory, Devansh Lab Werks, 234, Aquarius Drive, Homewood, Alabama, USA-3520.
  • Prachetha Kolli Scientist, Microgen Health Inc, 14225, Sullyfield Cir Suite E, Chantilly, VA, USA-2015
  • Dr.K.Venkata Gopaiah Associate Professor,St. Mary’s College of Pharmacy,Chebrolu, Guntur-A.P-522 212-India



SDR, PsPA, OFX, MIC, EF-Tu, EF-P, E. Coli


In the present study we observed on performing docking analysis that OFX interacted with conserved residues of Usp, SDR, PspA and CoA transferease domain of Rv2140c, Rv0148, Rv2744c and Rv3551, respectively, which might alter this function. It is predicted that these proteins might be exhibiting increased intensities to inhibit/modulate/compensate the effect of drugs. Further, detailed study in this direction might help to search new targets for drug development. Besides known proteins, upregulation of hypothetical proteins strengthen the possibility of some unknown underlying mechanism responsible for resistance to OFX. This could be crucial for the initial survival of the cells before gene level changes could come into play to ensure survival under prolonged adverse conditions. These findings may be further exploited to develop newer therapeutic agents derived from OFX. Further detailed and in-depth investigations to explore these leads will give an insight into probable sites of drug action, other than established primary sites and hence may help in the search of novel chemotherapeutic agents at these new sites as inhibitors and could provide the mankind with some ultimate treatmentstrategies.


Download data is not yet available.


Aagaard C, Hoang T, Dietrich J, Cardona PJ, Izzo A, Dolganov G, Schoolnik GK, Cassidy JP, Billeskov R and Anderson P (2011). A multistage tuberculosis vaccine that confers efficient protection before and after exposure. Nature Med 17:189–194.

Abel K and Jurnak F (1996). A complex profile of protein elongation:translating chemical energy into molecular movement. Structure4:229–238.

Aebersold RH, Teplow DB, Hood LE and Kent SB (1986). Electroblotting onto activated glass. High efficiency preparation of proteins from analytical sodium dodecyl sulfate-polyacrylamide gels for direct sequence analysis. J Biol Chem 261:4229-4238.

Agrawal GK, Rakwal R, Yonekura M, Kubo A and Saji H (2002). Proteome analysis of differentially displayed proteins as a tool for investigating ozone stress in rice (Oryza sativa L.) seedlings. Proteomics2:947-959.

Agrawal GK, Yonekura M, Iwahashi Y, Iwahashi H and Rakwal R (2005). System, trends and perspectives of proteomics in dicot plants Part III: Unraveling the proteomes influenced by the environment, and at the levels of function and genetic relationships. J Chromatography B 815: 137- 145.

Aicher L, Wahl D, Arce A, Grenet O and Steiner S (1998). New insights into cyclosporine A nephrotoxicity by proteome analysis. Electrophoresis 19:1998-2003.

Alen C and Sonenshein AL (1999). Bacillus subtilis aconitase is an RNAbinding protein. Proc Natl Acad Sci USA96:10412–10417.

Alms GR, Sanz P, Carlson M and Haystead TA (1999). Reg1p targets protein phosphatase 1 to dephosphorylate hexokinase II in Saccharomyces cerevisiae: characterizing the effects of a phosphatase subunit on the yeast proteome. EMBO J 18:4157-4168.

Altschul SF, Gish W, Miller W, Myers EW and Lipman DJ (1990). Basic local alignment search tool. J Mol Biol 215(3):403-410.

Andersen P (1994). Effective vaccination of mice against Mycobacterium tuberculosis infection with a soluble mixture of secreted mycobacterial proteins. Infect Immun 62:2536-2544.

AndersenP,AndersenAB,SorensenAlandNagaiS(1995).Recalloflong-livedimmunitytoMycobacterium tuberculosis infection in mice. J Immunol 154: 3359-3372.

Andersson T, Johansson M, Bolmsjo G and James P (2007). Automating MALDI sample plate loading. J Proteome Res 6:894-896.

Andrusier N, Nussinov R, Wolfson HJ (2007). FireDock: Fast interaction refinement in molecular docking. Proteins69(1):139-159.

Aoki H, Adams SL, Chung DG, Yaguchi M, Chuang SE and Ganoza MC (1991). "Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis." Nucleic acids research 19:6215-6220.

AranazAD,MateosCAandDomonguezL(2003).EvaluationofMycobacteriumtuberculosissubsp. caprae to species rank as M. caprae comp. nov. sp. Int J Syst Evol Microbiol 53: 1785-1789.

Armitige, LY, Jagannath C, Wanger AR and Norris SJ (2000). Disruption of the genes encoding antigen 85A and antigen 85B of Mycobacterium tuberculosis H37Rv: effect on growth in culture and in macrophages. Infect Immun 68:767-778.

Aubry A, Veziris N, Cambau E, Truffot-Pernot C, Jarlier V and Fisher LM (2006) Novel gyrase mutations in quinolone-resistant and -hypersusceptible clinical isolates of Mycobacterium tuberculosis: functional analysis of mutant enzymes. Antimicrob Agents Chemother 50:104–112.

Bai N, Pai M, Murthy P and Venkitasubramanian T (1982). Fructose-bisphosphate aldolases from mycobacteria. Methods Enzymol 90:241–250.

Bai NJ, Pai MR, Murthy PS and Venkitasubramanian TA (1974). Effect of oxygen tension on the aldolases of Mycobacterium tuberculosis H37Rv. FEBS Lett45:68–70.

Baird PN, Hall LM and Coates AR (1988). A major antigen from Mycobacterium tuberculosis which is homologous to heat shock proteins groES from E. coli and htpA gene product of Coxiella burneti. Nucleic Acids Res 16:9047.

Ball P (2000). Quinolone generations: natural history or natural selection? J AntimicrobChemother

a. 46(suppl T1): 17–24.

Banerjee S, Nandyala AK, Raviprasad P, Ahmed N and Hasnain SE (2007). Iron-Dependent RNA- Binding Activity of Mycobacterium tuberculosis Aconitase. J Bacteriol 189(11):4046–4052.

Barnes PF, Mehra V, Rivoire B, Fong SJ, Brennan PJ, Voegtline MS, Minden P, Houghten RA, Bloom BR and Modlin RL (1992). Immunoreactivity of a 10-kDa antigen of Mycobacterium tuberculosis. J Immunol148:1835–1840.

Bateman A, Murzin AG and Teichmann SA (1998). Structure and distribution of pentapeptide repeats in bacteria. Protein Sci7:1477–1480.

Beatty WL and Russell DG (2000). Identification of mycobacterial surface proteins released into subcellular compartments of infected macrophages. Infect Immun68(12):6997-7002.

Behar SM, Woodworth JSM and Wu Y (2007). The next generation: tuberculosis vaccines that elicit protective CD8+ T cells. Expert Rev Vaccines 6(3):441–456.

Belisle JT, Vissa VD, Sievert T, Takayama K, Brennan PJ, Besra GS (1997). Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis. Science 276:1420-1422.

Berning ES (2001). The role of fluoroquinolones in tuberculosis. Today:61-69.

Betts JC, Dodson P, Quan S, Lewis AP, Thomas PJ, Duncan K and McAdam RA (2000). Comparison of the proteome of Mycobacterium tuberculosis strain H37Rv with clinical isolate CDC 1551. Microbiology 146:3205-3216.

Betts JC, Lukey PT, Robb LC, McAdam RA and Duncan K (2002). Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol Microbio 43(3):717–731.


14 Views | 10 Downloads

How to Cite

Sudhakar Kancharla, Prachetha Kolli, and Dr.K.Venkata Gopaiah. “Selection of M. Tuberculosis Clinically Isolated Sensitive & Resistant to Fluoroquinolones ”. International Journal of Pharmaceutics and Drug Analysis, vol. 9, no. 1, Mar. 2021, pp. 15-23, doi:10.47957/ijpda.v9i1.453.



Research Articles
Share |